ID DJC16_HUMAN Reviewed; 782 AA. AC Q9Y2G8; Q68D57; Q86X32; Q8N5P4; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 3. DT 28-JAN-2026, entry version 168. DE RecName: Full=DnaJ homolog subfamily C member 16; DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 8 {ECO:0000303|PubMed:32492081}; DE Short=ER-resident protein ERdj8; DE Short=ERdj8; DE Flags: Precursor; GN Name=DNAJC16; Synonyms=ERDJ8, KIAA0962; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [2] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-57; CYS-171 AND RP CYS-174. RX PubMed=32492081; DOI=10.1083/jcb.201903127; RA Yamamoto Y.H., Kasai A., Omori H., Takino T., Sugihara M., Umemoto T., RA Hamasaki M., Hatta T., Natsume T., Morimoto R.I., Arai R., Waguri S., RA Sato M., Sato K., Bar-Nun S., Yoshimori T., Noda T., Nagata K.; RT "ERdj8 governs the size of autophagosomes during the formation process."; RL J. Cell Biol. 219:0-0(2020). CC -!- FUNCTION: Plays an important role in regulating the size of CC autophagosomes during the formation process. CC {ECO:0000269|PubMed:32492081}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:32492081}; Single-pass type IV membrane protein CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y2G8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y2G8-2; Sequence=VSP_018583; CC -!- SEQUENCE CAUTION: CC Sequence=BAA76806.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB023179; BAA76806.2; ALT_INIT; mRNA. DR EMBL; CR749259; CAH18115.1; -; mRNA. DR EMBL; CR749567; CAH18363.1; -; mRNA. DR EMBL; AL512883; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121992; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC031991; AAH31991.1; -; mRNA. DR EMBL; BC047363; AAH47363.1; -; mRNA. DR CCDS; CCDS30606.1; -. [Q9Y2G8-1] DR CCDS; CCDS72710.1; -. [Q9Y2G8-2] DR RefSeq; NP_001274740.1; NM_001287811.2. [Q9Y2G8-2] DR RefSeq; NP_056106.1; NM_015291.4. [Q9Y2G8-1] DR AlphaFoldDB; Q9Y2G8; -. DR SMR; Q9Y2G8; -. DR BioGRID; 116926; 288. DR FunCoup; Q9Y2G8; 1374. DR MINT; Q9Y2G8; -. DR STRING; 9606.ENSP00000365007; -. DR GlyCosmos; Q9Y2G8; 1 site, No reported glycans. DR GlyGen; Q9Y2G8; 1 site. DR iPTMnet; Q9Y2G8; -. DR PhosphoSitePlus; Q9Y2G8; -. DR SwissPalm; Q9Y2G8; -. DR BioMuta; DNAJC16; -. DR DMDM; 108936027; -. DR jPOST; Q9Y2G8; -. DR MassIVE; Q9Y2G8; -. DR PaxDb; 9606-ENSP00000365007; -. DR PeptideAtlas; Q9Y2G8; -. DR ProteomicsDB; 85773; -. [Q9Y2G8-1] DR ProteomicsDB; 85774; -. [Q9Y2G8-2] DR Pumba; Q9Y2G8; -. DR Antibodypedia; 46653; 28 antibodies from 14 providers. DR DNASU; 23341; -. DR Ensembl; ENST00000375847.8; ENSP00000365007.3; ENSG00000116138.14. [Q9Y2G8-1] DR Ensembl; ENST00000616884.4; ENSP00000480224.1; ENSG00000116138.14. [Q9Y2G8-2] DR GeneID; 23341; -. DR KEGG; hsa:23341; -. DR MANE-Select; ENST00000375847.8; ENSP00000365007.3; NM_015291.4; NP_056106.1. DR UCSC; uc001aws.4; human. [Q9Y2G8-1] DR AGR; HGNC:29157; -. DR ClinPGx; PA142671964; -. DR CTD; 23341; -. DR DisGeNET; 23341; -. DR GeneCards; DNAJC16; -. DR HGNC; HGNC:29157; DNAJC16. DR HPA; ENSG00000116138; Low tissue specificity. DR MIM; 619973; gene. DR OpenTargets; ENSG00000116138; -. DR VEuPathDB; HostDB:ENSG00000116138; -. DR eggNOG; KOG0715; Eukaryota. DR GeneTree; ENSGT00940000155851; -. DR HOGENOM; CLU_020140_0_1_1; -. DR InParanoid; Q9Y2G8; -. DR OMA; QPEFAST; -. DR OrthoDB; 10065037at2759; -. DR PAN-GO; Q9Y2G8; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q9Y2G8; -. DR PathwayCommons; Q9Y2G8; -. DR SignaLink; Q9Y2G8; -. DR Agora; ENSG00000116138; -. DR BioGRID-ORCS; 23341; 19 hits in 1157 CRISPR screens. DR ChiTaRS; DNAJC16; human. DR GenomeRNAi; 23341; -. DR Pharos; Q9Y2G8; Tdark. DR PRO; PR:Q9Y2G8; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y2G8; protein. DR Bgee; ENSG00000116138; Expressed in right lobe of liver and 205 other cell types or tissues. DR ExpressionAtlas; Q9Y2G8; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016243; P:regulation of autophagosome size; IMP:UniProtKB. DR CDD; cd06257; DnaJ; 1. DR CDD; cd02963; TRX_DnaJ; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR052448; DnaJ_C16_autophagy_reg. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR InterPro; IPR043361; DNAJC16_TRX. DR InterPro; IPR036869; J_dom_sf. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR44303; DNAJ HOMOLOG SUBFAMILY C MEMBER 16; 1. DR PANTHER; PTHR44303:SF2; DNAJ HOMOLOG SUBFAMILY C MEMBER 16; 1. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF00085; Thioredoxin; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; Chaperone J-domain; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Autophagy; Endoplasmic reticulum; Glycoprotein; KW Membrane; Proteomics identification; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..782 FT /note="DnaJ homolog subfamily C member 16" FT /id="PRO_0000236683" FT TOPO_DOM 26..535 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 536..556 FT /note="Helical; Anchor for type IV membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 557..782 FT /note="Extracellular" FT /evidence="ECO:0000255" FT DOMAIN 29..93 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT DOMAIN 119..247 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT REGION 562..593 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 563..582 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 583..593 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 631 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..312 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_018583" FT MUTAGEN 57 FT /note="H->Q: Does not lead to enlargement of autophagosomes FT when overexpressed." FT /evidence="ECO:0000269|PubMed:32492081" FT MUTAGEN 171 FT /note="C->A: Does not lead to enlargement of autophagosomes FT when overexpressed; when associated with A-174." FT /evidence="ECO:0000269|PubMed:32492081" FT MUTAGEN 174 FT /note="C->A: Does not lead to enlargement of autophagosomes FT when overexpressed; when associated with A-171." FT /evidence="ECO:0000269|PubMed:32492081" SQ SEQUENCE 782 AA; 90591 MW; 42D564BBC6EED981 CRC64; MEVRKLSISW QFLIVLVLIL QILSALDFDP YRVLGVSRTA SQADIKKAYK KLAREWHPDK NKDPGAEDKF IQISKAYEIL SNEEKRSNYD QYGDAGENQG YQKQQQQREY RFRHFHENFY FDESFFHFPF NSERRDSIDE KYLLHFSHYV NEVVPDSFKK PYLIKITSDW CFSCIHIEPV WKEVIQELEE LGVGIGVVHA GYERRLAHHL GAHSTPSILG IINGKISFFH NAVVRENLRQ FVESLLPGNL VEKVTNKNYV RFLSGWQQEN KPHVLLFDQT PIVPLLYKLT AFAYKDYLSF GYVYVGLRGT EEMTRRYNIN IYAPTLLVFK EHINRPADVI QARGMKKQII DDFITRNKYL LAARLTSQKL FHELCPVKRS HRQRKYCVVL LTAETTKLSK PFEAFLSFAL ANTQDTVRFV HVYSNRQQEF ADTLLPDSEA FQGKSAVSIL ERRNTAGRVV YKTLEDPWIG SESDKFILLG YLDQLRKDPA LLSSEAVLPD LTDELAPVFL LRWFYSASDY ISDCWDSIFH NNWREMMPLL SLIFSALFIL FGTVIVQAFS DSNDERESSP PEKEEAQEKT GKTEPSFTKE NSSKIPKKGF VEVTELTDVT YTSNLVRLRP GHMNVVLILS NSTKTSLLQK FALEVYTFTG SSCLHFSFLS LDKHREWLEY LLEFAQDAAP IPNQYDKHFM ERDYTGYVLA LNGHKKYFCL FKPQKTVEEE EAIGSCSDVD SSLYLGESRG KPSCGLGSRP IKGKLSKLSL WMERLLEGSL QRFYIPSWPE LD //